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-induced apoptosis in
cultured fibroblasts
3 Section of Pulmonary and Critical Care Medicine, Yale University School of Medicine, New Haven 06250; 4 Connecticut Veterans Affairs HealthCare Service, West Haven, Connecticut 06516; 2 Department of Molecular Genetics, Alton Ochsner Medical Foundation, and Department of Biochemistry and Molecular Biology, Louisiana State University Medical Center, New Orleans, Louisiana 70121; and 1 The Johns Hopkins Medical Institution, Baltimore, Maryland 21205
Heme oxygenase (HO)-1
catalyzes the oxidative cleavage of heme to yield equimolar amounts of
biliverdin, iron, and carbon monoxide. HO-1 is a stress response
protein, the induction of which is associated with protection against
oxidative stress. The mechanism(s) of protection is not completely
elucidated, although it is suggested that one or more of the catalytic
by-products provide antioxidant functions either directly or
indirectly. The involvement of reactive oxygen species in apoptosis
raised the question of a possible role for HO-1 in programmed cell
death. Using the tetracycline-regulated expression system, we show here that conditional overexpression of HO-1 prevents tumor necrosis factor-
-induced apoptosis in murine L929 fibroblasts. Inhibition of
apoptosis was not observed in the presence of tin protoporphyrin, a
specific inhibitor of HO activity, and in cells overexpressing antisense HO-1. Interestingly, exogenous administration of a low concentration of carbon monoxide also prevented tumor necrosis factor--induced apoptosis in L929 fibroblasts. Inhibition of tumor
necrosis factor--induced apoptosis by HO-1 overexpression was
reversed by
1H-(1,2,4)oxadiazolo(4,3-a)quinoxalin-1-one, an inhibitor of guanylate cyclase, which is a target enzyme for carbon monoxide. Taken together, our data suggest that the antiapoptotic effect of HO-1 may be mediated via carbon monoxide.
tumor necrosis factor-; programmed cell death; carbon monoxide; oxidants; reactive oxygen species
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